Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.febslet.2004.12.041 (literal)

Alternative label

• M. Maiorino, P.L. Mauri, A. Roveri, L. Benazzi, S. Toppo, V. Bosello F. Ursini (2005)
  Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa
  in FEBS letters (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• M. Maiorino, P.L. Mauri, A. Roveri, L. Benazzi, S. Toppo, V. Bosello F. Ursini (literal)

Pagina inizio

• 667 (literal)

Pagina fine

• 670 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 579 (literal)

Rivista

• FEBS letters (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 3 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• ITB-CNR Università di Padova (literal)

Titolo

• Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa (literal)

Abstract

• Phospholipid hydroperoxide glutathione peroxidase is a monomeric Se-peroxidase highly expressed in mammalian male germ cells. Its nuclear form, sperm nuclei glutathione peroxidase (snGPx), has been originally identified in maturating spermatozoa as a transcription product containing an alternative exon within the phospholipid hydroperoxide glutathione peroxidase gene. In this paper, we show that this form is inconstantly detectable in rat spermatozoa where a 20.0 and 25.9 kDa major forms are detected instead. These have been conclusively characterized. The N-terminus sequence of the 20.0 kDa form confirmed that the protein is identical to cytosolic form, suggesting diffusion into the nucleus. The 25.9 kDa protein represented a truncated form of the previously described nuclear snGPx, lacking the basic nuclear localization signal. This protein is present in two forms differing from each other by the presence of an N-terminal methionine. The presence of traces of the larger snGPx form suggests that exhaustive proteolytic processing of the precursor produces the 25.9 kDa enzyme, although the alternate use of a downstream ATG, at least in rodents, could not be unequivocally ruled out. (C) 2004 Federation of European Biochemical Societies. (literal)

Prodotto di

• ProteoMetabolomica - Sviluppo ed applicazione della LC-MS/MS per lo studio di proteine e metaboliti (PM.P06.008.003) (Modulo)

Autore CNR

• PIETRO LUIGI MAURI (Unità di personale interno)
• LOUISE BENAZZI (Persona)

Insieme di parole chiave

• Keywords of "Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• LOUISE BENAZZI (Persona)
• PIETRO LUIGI MAURI (Unità di personale interno)

Prodotto

• ProteoMetabolomica - Sviluppo ed applicazione della LC-MS/MS per lo studio di proteine e metaboliti (PM.P06.008.003) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• FEBS letters (Rivista)

Insieme di parole chiave di

• Keywords of "Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa" (Insieme di parole chiave)